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T. Springer, Michael Dustin, T. Kishimoto, S. Marlin (1987)
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The primary structure of the beta‐subunit of the cell surface adhesion glycoproteins LFA‐1, CR3 and p150,95 and its relationship to the fibronectin receptor.The EMBO Journal, 6
L. Miller, M. Wiebe, T. Springer (1987)
Purification and alpha subunit N-terminal sequences of human Mac-1 and p150,95 leukocyte adhesion proteins.Journal of immunology, 138 8
M. Patarroyo, E. Clark, J. Prieto, C. Kantor, C. Gahmberg (1987)
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Cell-cell adhesion is essential for many immunological functions1–4. The LFA-1 molecule, a member of a superfamily of adhesion molecules, participates in adhesion which is critical to the function of each of the three major subsets of leukocytes: lymphocytes, monocytes and granulocytes5. Putative LFA-1 ligands have been identified functionally in different laboratories using three different monoclonal antibodies that inhibit LFA-1-mediated leukocyte adhesion in particular model systems; however, there may be more than one LFA-1 ligand6–8. We have directly compared the three relevant monoclonal antibodies, and show that each binds to the same molecule, intercellular-adhesion molecule-1 (ICAM-1). Most important, B, T and myeloid cells adhere specifically to purified ICAM-1-coated surfaces; such adhesion has distinctive requirements for Mg2+ and Ca2+. This constitutes biochemical evidence that ICAM-1 functions as a ligand for LFA-1-dependent adhesion by a variety of leukocytes.
Nature – Springer Journals
Published: Jan 7, 1988
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